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Q09013

- DMPK_HUMAN

UniProt

Q09013 - DMPK_HUMAN

Protein

Myotonin-protein kinase

Gene

DMPK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 3 (14 Dec 2011)
      Previous versions | rss
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    Functioni

    Non-receptor serine/threonine protein kinase which is necessary for the maintenance of skeletal muscle structure and function. May play a role in myocyte differentiation and survival by regulating the integrity of the nuclear envelope and the expression of muscle-specific genes. May also phosphorylate PPP1R12A and inhibit the myosin phosphatase activity to regulate myosin phosphorylation. Also critical to the modulation of cardiac contractility and to the maintenance of proper cardiac conduction activity probably through the regulation of cellular calcium homeostasis. Phosphorylates PLN, a regulator of calcium pumps and may regulate sarcoplasmic reticulum calcium uptake in myocytes. May also phosphorylate FXYD1/PLM which is able to induce chloride currents. May also play a role in synaptic plasticity.6 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Coiled-coil-mediated oligomerization enhances the catalytic activity. Proteolytic processing of the C-terminus may release the protein from membranes and constitute a mean to regulate the enzyme. May be regulated by HSPB2, RAC1, RAF1 and G-protein second messengers.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei100 – 1001ATP
    Active sitei195 – 1951Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi77 – 859ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. myosin phosphatase regulator activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. cellular calcium ion homeostasis Source: UniProtKB
    2. muscle cell apoptotic process Source: UniProtKB
    3. nuclear envelope organization Source: UniProtKB
    4. protein phosphorylation Source: UniProtKB
    5. regulation of catalytic activity Source: GOC
    6. regulation of excitatory postsynaptic membrane potential involved in skeletal muscle contraction Source: Ensembl
    7. regulation of heart contraction Source: UniProtKB
    8. regulation of myotube differentiation Source: UniProtKB
    9. regulation of skeletal muscle contraction by calcium ion signaling Source: Ensembl
    10. regulation of sodium ion transport Source: Ensembl
    11. regulation of synapse structural plasticity Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    SignaLinkiQ09013.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myotonin-protein kinase (EC:2.7.11.1)
    Short name:
    MT-PK
    Alternative name(s):
    DM-kinase
    Short name:
    DMK
    DM1 protein kinase
    DMPK
    Myotonic dystrophy protein kinase
    Gene namesi
    Name:DMPK
    Synonyms:DM1PK, MDPK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:2933. DMPK.

    Subcellular locationi

    Endoplasmic reticulum membrane By similarity; Single-pass type IV membrane protein By similarity; Cytoplasmic side By similarity. Nucleus outer membrane Curated; Single-pass type IV membrane protein Curated; Cytoplasmic side Curated. Mitochondrion outer membrane Curated; Single-pass type IV membrane protein Curated. Sarcoplasmic reticulum membrane By similarity. Cell membrane By similarity. Cytoplasmcytosol By similarity
    Note: Localizes to sarcoplasmic reticulum membranes of cardiomyocytes.By similarity

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. endoplasmic reticulum membrane Source: UniProtKB
    3. integral component of mitochondrial outer membrane Source: UniProtKB
    4. nuclear membrane Source: UniProtKB
    5. nuclear outer membrane Source: UniProtKB-SubCell
    6. plasma membrane Source: UniProtKB
    7. sarcoplasmic reticulum membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus, Sarcoplasmic reticulum

    Pathology & Biotechi

    Involvement in diseasei

    Dystrophia myotonica 1 (DM1) [MIM:160900]: A muscular disorder characterized by myotonia, muscle wasting in the distal extremities, cataract, hypogonadism, defective endocrine functions, male baldness and cardiac arrhythmias.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry. The causative mutation is a CTG expansion in the 3'-UTR of the DMPK gene. A length exceeding 50 CTG repeats is pathogenic, while normal individuals have 5 to 37 repeats. Intermediate alleles with 35-49 triplets are not disease-causing but show instability in intergenerational transmissions. Disease severity varies with the number of repeats: mildly affected persons have 50 to 150 repeats, patients with classic DM have 100 to 1,000 repeats, and those with congenital onset can have more than 2,000 repeats.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi100 – 1001K → A: Loss of kinase activity. 1 Publication

    Keywords - Diseasei

    Cataract

    Organism-specific databases

    MIMi160900. phenotype.
    Orphaneti273. Steinert myotonic dystrophy.
    PharmGKBiPA27380.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 629629Myotonin-protein kinasePRO_0000085924Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei216 – 2161Phosphoserine; by autocatalysisBy similarity
    Modified residuei228 – 2281Phosphoserine; by autocatalysisBy similarity
    Modified residuei234 – 2341Phosphothreonine; by autocatalysisBy similarity

    Post-translational modificationi

    Phosphorylated. Autophosphorylates. Phosphorylation by RAF1 may result in activation of DMPK.1 Publication
    Proteolytic processing of the C-terminus may remove the transmembrane domain and release the kinase from membranes stimulating its activity.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ09013.
    PRIDEiQ09013.

    2D gel databases

    REPRODUCTION-2DPAGEQ09013.

    PTM databases

    PhosphoSiteiQ09013.

    Expressioni

    Tissue specificityi

    Most isoforms are expressed in many tissues including heart, skeletal muscle, liver and brain, except for isoform 2 which is only found in the heart and skeletal muscle, and isoform 14 which is only found in the brain, with high levels in the striatum, cerebellar cortex and pons.1 Publication

    Gene expression databases

    ArrayExpressiQ09013.
    BgeeiQ09013.
    CleanExiHS_DMPK.
    GenevestigatoriQ09013.

    Organism-specific databases

    HPAiHPA007164.
    HPA008905.

    Interactioni

    Subunit structurei

    Homodimer; homodimerization stimulates the kinase activity. Interacts with HSPB2; may enhance DMPK kinase activity. Interacts with PLN; phosphorylates PLN. May interact with RAC1; may regulate DMPK kinase activity. Interacts with LMNA; may regulate nuclear envelope stability.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PLNP266784EBI-692774,EBI-692836

    Protein-protein interaction databases

    BioGridi108100. 15 interactions.
    IntActiQ09013. 15 interactions.
    MINTiMINT-195910.
    STRINGi9606.ENSP00000345997.

    Structurei

    Secondary structure

    1
    629
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi12 – 154
    Turni17 – 193
    Helixi22 – 3716
    Helixi40 – 434
    Helixi45 – 6420
    Helixi68 – 703
    Beta strandi71 – 799
    Beta strandi84 – 907
    Turni91 – 933
    Beta strandi96 – 1038
    Helixi104 – 1107
    Helixi111 – 1133
    Helixi116 – 12510
    Turni128 – 1303
    Beta strandi134 – 1396
    Beta strandi141 – 1488
    Helixi156 – 1638
    Helixi169 – 18820
    Helixi198 – 2003
    Beta strandi201 – 2033
    Beta strandi209 – 2113
    Helixi235 – 2373
    Helixi240 – 2478
    Beta strandi253 – 2553
    Helixi258 – 27316
    Helixi283 – 2919
    Helixi293 – 2964
    Helixi308 – 3158
    Helixi321 – 3233
    Turni325 – 3295
    Helixi330 – 3345
    Helixi337 – 3393
    Beta strandi378 – 3825
    Turni385 – 3873
    Helixi398 – 4003
    Helixi412 – 4143
    Helixi468 – 52861

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WT6X-ray1.60A/B/D460-537[»]
    2VD5X-ray2.80A/B11-420[»]
    ProteinModelPortaliQ09013.
    SMRiQ09013. Positions 11-416, 461-527.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ09013.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 590590CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini612 – 62918LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei591 – 61121Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini71 – 339269Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini340 – 41576AGC-kinase C-terminalAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili457 – 536802 PublicationsAdd
    BLAST

    Domaini

    The coiled coil domain is required for homodimerization and regulates the enzymatic activity.

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233033.
    HOVERGENiHBG107817.
    KOiK08788.
    OMAiTHCNISS.
    OrthoDBiEOG7F511X.
    TreeFamiTF105337.

    Family and domain databases

    InterProiIPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR014930. Myotonic_dystrophy_kinase_coil.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF08826. DMPK_coil. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    ProDomiPD011252. Myotonic_dystrophy_kinase_coil. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (12)i

    Sequence statusi: Complete.

    This entry describes 12 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q09013-9) [UniParc]FASTAAdd to Basket

    Also known as: DMPK A

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSAEVRLRRL QQLVLDPGFL GLEPLLDLLL GVHQELGASE LAQDKYVADF    50
    LQWAEPIVVR LKEVRLQRDD FEILKVIGRG AFSEVAVVKM KQTGQVYAMK 100
    IMNKWDMLKR GEVSCFREER DVLVNGDRRW ITQLHFAFQD ENYLYLVMEY 150
    YVGGDLLTLL SKFGERIPAE MARFYLAEIV MAIDSVHRLG YVHRDIKPDN 200
    ILLDRCGHIR LADFGSCLKL RADGTVRSLV AVGTPDYLSP EILQAVGGGP 250
    GTGSYGPECD WWALGVFAYE MFYGQTPFYA DSTAETYGKI VHYKEHLSLP 300
    LVDEGVPEEA RDFIQRLLCP PETRLGRGGA GDFRTHPFFF GLDWDGLRDS 350
    VPPFTPDFEG ATDTCNFDLV EDGLTAMVSG GGETLSDIRE GAPLGVHLPF 400
    VGYSYSCMAL RDSEVPGPTP MELEAEQLLE PHVQAPSLEP SVSPQDETAE 450
    VAVPAAVPAA EAEAEVTLRE LQEALEEEVL TRQSLSREME AIRTDNQNFA 500
    SQLREAEARN RDLEAHVRQL QERMELLQAE GATAVTGVPS PRATDPPSHL 550
    DGPPAVAVGQ CPLVGPGPMH RRHLLLPARV PRPGLSEALS LLLFAVVLSR 600
    AAALGCIGLV AHAGQLTAVW RRPGAARAP 629
    Length:629
    Mass (Da):69,385
    Last modified:December 14, 2011 - v3
    Checksum:i46783ED4AE65B493
    GO
    Isoform 2 (identifier: Q09013-11) [UniParc]FASTAAdd to Basket

    Also known as: DMPK B

    The sequence of this isoform differs from the canonical sequence as follows:
         378-382: Missing.

    Show »
    Length:624
    Mass (Da):69,028
    Checksum:i7ECA31ED9A84E7E1
    GO
    Isoform 3 (identifier: Q09013-16) [UniParc]FASTAAdd to Basket

    Also known as: DMPK C

    The sequence of this isoform differs from the canonical sequence as follows:
         550-629: LDGPPAVAVG...WRRPGAARAP → MAPRPWLWAS...AQEPPALPEP

    Note: No experimental confirmation available.

    Show »
    Length:630
    Mass (Da):69,950
    Checksum:i52B2B388CD99AA2F
    GO
    Isoform 4 (identifier: Q09013-15) [UniParc]FASTAAdd to Basket

    Also known as: DMPK D

    The sequence of this isoform differs from the canonical sequence as follows:
         378-382: Missing.
         550-629: LDGPPAVAVG...WRRPGAARAP → MAPRPWLWAS...AQEPPALPEP

    Show »
    Length:625
    Mass (Da):69,592
    Checksum:i10EA0187F4AD4B7C
    GO
    Isoform 5 (identifier: Q09013-10) [UniParc]FASTAAdd to Basket

    Also known as: DMPK E

    The sequence of this isoform differs from the canonical sequence as follows:
         534-535: AV → GP
         536-629: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:535
    Mass (Da):59,804
    Checksum:i9A08CEA02FAE8828
    GO
    Isoform 6 (identifier: Q09013-12) [UniParc]FASTAAdd to Basket

    Also known as: DMPK F

    The sequence of this isoform differs from the canonical sequence as follows:
         378-382: Missing.
         534-535: AV → GP
         536-629: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:530
    Mass (Da):59,446
    Checksum:i5E41498FDA6C22D4
    GO
    Isoform 7 (identifier: Q09013-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP

    Show »
    Length:639
    Mass (Da):70,371
    Checksum:i69A831604F7F8D38
    GO
    Isoform 8 (identifier: Q09013-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-89: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:540
    Mass (Da):59,334
    Checksum:iA7BB715CB845055C
    GO
    Isoform 9 (identifier: Q09013-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP
         226-275: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:589
    Mass (Da):65,076
    Checksum:i2558F658CFA1FCE1
    GO
    Isoform 10 (identifier: Q09013-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP
         378-382: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:634
    Mass (Da):70,014
    Checksum:i94F39ADE9A8F4AFC
    GO
    Isoform 11 (identifier: Q09013-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP
         550-579: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:609
    Mass (Da):67,263
    Checksum:i58A97059F9590719
    GO
    Isoform 12 (identifier: Q09013-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP
         534-535: AV → GP
         536-629: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:545
    Mass (Da):60,790
    Checksum:iEF016FDBE3933553
    GO

    Sequence cautioni

    The sequence AAA87583.1 differs from that shown. Reason: Probable cloning artifact.
    The sequence AAA64884.1 differs from that shown. Reason: Frameshift at positions 56, 555 and 568.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti474 – 4741A → P in AAB31800. (PubMed:8076686)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti423 – 4231L → V.4 Publications
    Corresponds to variant rs527221 [ dbSNP | Ensembl ].
    VAR_058334
    Natural varianti428 – 4281L → V in a lung small cell carcinoma sample; somatic mutation. 1 Publication
    VAR_040452

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8989Missing in isoform 8. CuratedVSP_042098Add
    BLAST
    Alternative sequencei1 – 5353MSAEV…DFLQW → MGGHFWPPEPYTVFMWGSPW EADSPRVKLRGREKGRQTEG GAFPLVSSALSGDPRFFSPT TPP in isoform 7, isoform 9, isoform 10, isoform 11 and isoform 12. 2 PublicationsVSP_042099Add
    BLAST
    Alternative sequencei226 – 27550Missing in isoform 9. CuratedVSP_042100Add
    BLAST
    Alternative sequencei378 – 3825Missing in isoform 2, isoform 4, isoform 6 and isoform 10. 3 PublicationsVSP_042101
    Alternative sequencei534 – 5352AV → GP in isoform 5, isoform 6 and isoform 12. CuratedVSP_042102
    Alternative sequencei536 – 62994Missing in isoform 5, isoform 6 and isoform 12. CuratedVSP_042103Add
    BLAST
    Alternative sequencei550 – 62980LDGPP…AARAP → MAPRPWLWASARWWGQAPCT AATCCSLPGSLGLAYRRRFP CSCSPLFCLVPPPWAALGWW PTPANSPQSGAAQEPPALPE P in isoform 3 and isoform 4. 1 PublicationVSP_042104Add
    BLAST
    Alternative sequencei550 – 57930Missing in isoform 11. CuratedVSP_042105Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M87312 mRNA. No translation available.
    L19268 mRNA. Translation: AAA36206.1.
    L19266 Genomic DNA. Translation: AAA36205.1.
    L08835 Genomic DNA. Translation: AAC14449.1.
    L08835 Genomic DNA. Translation: AAC14451.1.
    L08835 Genomic DNA. Translation: AAC14448.1.
    L08835 Genomic DNA. Translation: AAC14450.1.
    L00727 Genomic DNA. Translation: AAA75235.1.
    L00727 Genomic DNA. Translation: AAA75236.1.
    L00727 Genomic DNA. Translation: AAA75237.1.
    L00727 Genomic DNA. Translation: AAA75238.1.
    L00727 Genomic DNA. Translation: AAA75239.1.
    L00727 Genomic DNA. Translation: AAA75240.1.
    S72883 mRNA. Translation: AAB31800.1.
    HQ205626 Genomic DNA. Translation: ADP91337.1.
    HQ205627 Genomic DNA. Translation: ADP91341.1.
    HQ205628 Genomic DNA. Translation: ADP91345.1.
    HQ205629 Genomic DNA. Translation: ADP91349.1.
    HQ205630 Genomic DNA. Translation: ADP91353.1.
    HQ205631 Genomic DNA. Translation: ADP91357.1.
    HQ205632 Genomic DNA. Translation: ADP91361.1.
    HQ205633 Genomic DNA. Translation: ADP91365.1.
    HQ205634 Genomic DNA. Translation: ADP91369.1.
    HQ205635 Genomic DNA. Translation: ADP91373.1.
    HQ205636 Genomic DNA. Translation: ADP91377.1.
    HQ205637 Genomic DNA. Translation: ADP91381.1.
    HQ205638 Genomic DNA. Translation: ADP91385.1.
    HQ205639 Genomic DNA. Translation: ADP91389.1.
    HQ205640 Genomic DNA. Translation: ADP91393.1.
    HQ205641 Genomic DNA. Translation: ADP91397.1.
    HQ205642 Genomic DNA. Translation: ADP91401.1.
    HQ205643 Genomic DNA. Translation: ADP91405.1.
    HQ205644 Genomic DNA. Translation: ADP91409.1.
    HQ205645 Genomic DNA. Translation: ADP91413.1.
    HQ205646 Genomic DNA. Translation: ADP91417.1.
    HQ205647 Genomic DNA. Translation: ADP91421.1.
    HQ205648 Genomic DNA. Translation: ADP91425.1.
    HQ205649 Genomic DNA. Translation: ADP91429.1.
    HQ205650 Genomic DNA. Translation: ADP91433.1.
    HQ205651 Genomic DNA. Translation: ADP91437.1.
    HQ205652 Genomic DNA. Translation: ADP91441.1.
    HQ205653 Genomic DNA. Translation: ADP91445.1.
    HQ205654 Genomic DNA. Translation: ADP91449.1.
    HQ205655 Genomic DNA. Translation: ADP91453.1.
    HQ205656 Genomic DNA. Translation: ADP91457.1.
    HQ205657 Genomic DNA. Translation: ADP91461.1.
    HQ205658 Genomic DNA. Translation: ADP91465.1.
    HQ205659 Genomic DNA. Translation: ADP91469.1.
    HQ205660 Genomic DNA. Translation: ADP91473.1.
    HQ205661 Genomic DNA. Translation: ADP91477.1.
    HQ205662 Genomic DNA. Translation: ADP91481.1.
    HQ205663 Genomic DNA. Translation: ADP91485.1.
    HQ205664 Genomic DNA. Translation: ADP91489.1.
    HQ205665 Genomic DNA. Translation: ADP91493.1.
    KJ534827 mRNA. Translation: AHW56467.1.
    CH471126 Genomic DNA. Translation: EAW57380.1.
    CH471126 Genomic DNA. Translation: EAW57382.1.
    BC062553 mRNA. Translation: AAH62553.1.
    M94203 mRNA. Translation: AAA64884.1. Frameshift.
    U46546 mRNA. Translation: AAA87583.1. Sequence problems.
    CCDSiCCDS12674.1. [Q09013-9]
    CCDS46117.1. [Q09013-15]
    CCDS46118.1. [Q09013-11]
    CCDS46119.1. [Q09013-1]
    PIRiB49364.
    RefSeqiNP_001075029.1. NM_001081560.2. [Q09013-11]
    NP_001075031.1. NM_001081562.2. [Q09013-15]
    NP_001075032.1. NM_001081563.2. [Q09013-1]
    NP_001275694.1. NM_001288765.1.
    NP_004400.4. NM_004409.4. [Q09013-9]
    UniGeneiHs.631596.

    Genome annotation databases

    GeneIDi1760.
    KEGGihsa:1760.
    UCSCiuc002pdf.1. human. [Q09013-9]
    uc010xxs.1. human. [Q09013-16]
    uc010xxt.1. human. [Q09013-12]

    Polymorphism databases

    DMDMi363548519.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M87312 mRNA. No translation available.
    L19268 mRNA. Translation: AAA36206.1 .
    L19266 Genomic DNA. Translation: AAA36205.1 .
    L08835 Genomic DNA. Translation: AAC14449.1 .
    L08835 Genomic DNA. Translation: AAC14451.1 .
    L08835 Genomic DNA. Translation: AAC14448.1 .
    L08835 Genomic DNA. Translation: AAC14450.1 .
    L00727 Genomic DNA. Translation: AAA75235.1 .
    L00727 Genomic DNA. Translation: AAA75236.1 .
    L00727 Genomic DNA. Translation: AAA75237.1 .
    L00727 Genomic DNA. Translation: AAA75238.1 .
    L00727 Genomic DNA. Translation: AAA75239.1 .
    L00727 Genomic DNA. Translation: AAA75240.1 .
    S72883 mRNA. Translation: AAB31800.1 .
    HQ205626 Genomic DNA. Translation: ADP91337.1 .
    HQ205627 Genomic DNA. Translation: ADP91341.1 .
    HQ205628 Genomic DNA. Translation: ADP91345.1 .
    HQ205629 Genomic DNA. Translation: ADP91349.1 .
    HQ205630 Genomic DNA. Translation: ADP91353.1 .
    HQ205631 Genomic DNA. Translation: ADP91357.1 .
    HQ205632 Genomic DNA. Translation: ADP91361.1 .
    HQ205633 Genomic DNA. Translation: ADP91365.1 .
    HQ205634 Genomic DNA. Translation: ADP91369.1 .
    HQ205635 Genomic DNA. Translation: ADP91373.1 .
    HQ205636 Genomic DNA. Translation: ADP91377.1 .
    HQ205637 Genomic DNA. Translation: ADP91381.1 .
    HQ205638 Genomic DNA. Translation: ADP91385.1 .
    HQ205639 Genomic DNA. Translation: ADP91389.1 .
    HQ205640 Genomic DNA. Translation: ADP91393.1 .
    HQ205641 Genomic DNA. Translation: ADP91397.1 .
    HQ205642 Genomic DNA. Translation: ADP91401.1 .
    HQ205643 Genomic DNA. Translation: ADP91405.1 .
    HQ205644 Genomic DNA. Translation: ADP91409.1 .
    HQ205645 Genomic DNA. Translation: ADP91413.1 .
    HQ205646 Genomic DNA. Translation: ADP91417.1 .
    HQ205647 Genomic DNA. Translation: ADP91421.1 .
    HQ205648 Genomic DNA. Translation: ADP91425.1 .
    HQ205649 Genomic DNA. Translation: ADP91429.1 .
    HQ205650 Genomic DNA. Translation: ADP91433.1 .
    HQ205651 Genomic DNA. Translation: ADP91437.1 .
    HQ205652 Genomic DNA. Translation: ADP91441.1 .
    HQ205653 Genomic DNA. Translation: ADP91445.1 .
    HQ205654 Genomic DNA. Translation: ADP91449.1 .
    HQ205655 Genomic DNA. Translation: ADP91453.1 .
    HQ205656 Genomic DNA. Translation: ADP91457.1 .
    HQ205657 Genomic DNA. Translation: ADP91461.1 .
    HQ205658 Genomic DNA. Translation: ADP91465.1 .
    HQ205659 Genomic DNA. Translation: ADP91469.1 .
    HQ205660 Genomic DNA. Translation: ADP91473.1 .
    HQ205661 Genomic DNA. Translation: ADP91477.1 .
    HQ205662 Genomic DNA. Translation: ADP91481.1 .
    HQ205663 Genomic DNA. Translation: ADP91485.1 .
    HQ205664 Genomic DNA. Translation: ADP91489.1 .
    HQ205665 Genomic DNA. Translation: ADP91493.1 .
    KJ534827 mRNA. Translation: AHW56467.1 .
    CH471126 Genomic DNA. Translation: EAW57380.1 .
    CH471126 Genomic DNA. Translation: EAW57382.1 .
    BC062553 mRNA. Translation: AAH62553.1 .
    M94203 mRNA. Translation: AAA64884.1 . Frameshift.
    U46546 mRNA. Translation: AAA87583.1 . Sequence problems.
    CCDSi CCDS12674.1. [Q09013-9 ]
    CCDS46117.1. [Q09013-15 ]
    CCDS46118.1. [Q09013-11 ]
    CCDS46119.1. [Q09013-1 ]
    PIRi B49364.
    RefSeqi NP_001075029.1. NM_001081560.2. [Q09013-11 ]
    NP_001075031.1. NM_001081562.2. [Q09013-15 ]
    NP_001075032.1. NM_001081563.2. [Q09013-1 ]
    NP_001275694.1. NM_001288765.1.
    NP_004400.4. NM_004409.4. [Q09013-9 ]
    UniGenei Hs.631596.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WT6 X-ray 1.60 A/B/D 460-537 [» ]
    2VD5 X-ray 2.80 A/B 11-420 [» ]
    ProteinModelPortali Q09013.
    SMRi Q09013. Positions 11-416, 461-527.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108100. 15 interactions.
    IntActi Q09013. 15 interactions.
    MINTi MINT-195910.
    STRINGi 9606.ENSP00000345997.

    Chemistry

    BindingDBi Q09013.
    ChEMBLi CHEMBL5320.
    GuidetoPHARMACOLOGYi 1505.

    PTM databases

    PhosphoSitei Q09013.

    Polymorphism databases

    DMDMi 363548519.

    2D gel databases

    REPRODUCTION-2DPAGE Q09013.

    Proteomic databases

    PaxDbi Q09013.
    PRIDEi Q09013.

    Protocols and materials databases

    DNASUi 1760.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1760.
    KEGGi hsa:1760.
    UCSCi uc002pdf.1. human. [Q09013-9 ]
    uc010xxs.1. human. [Q09013-16 ]
    uc010xxt.1. human. [Q09013-12 ]

    Organism-specific databases

    CTDi 1760.
    GeneCardsi GC19M046272.
    GeneReviewsi DMPK.
    H-InvDB HIX0137522.
    HGNCi HGNC:2933. DMPK.
    HPAi HPA007164.
    HPA008905.
    MIMi 160900. phenotype.
    605377. gene.
    neXtProti NX_Q09013.
    Orphaneti 273. Steinert myotonic dystrophy.
    PharmGKBi PA27380.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233033.
    HOVERGENi HBG107817.
    KOi K08788.
    OMAi THCNISS.
    OrthoDBi EOG7F511X.
    TreeFami TF105337.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    SignaLinki Q09013.

    Miscellaneous databases

    ChiTaRSi DMPK. human.
    EvolutionaryTracei Q09013.
    GeneWikii Myotonin-protein_kinase.
    GenomeRNAii 1760.
    NextBioi 7169.
    PROi Q09013.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q09013.
    Bgeei Q09013.
    CleanExi HS_DMPK.
    Genevestigatori Q09013.

    Family and domain databases

    InterProi IPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR014930. Myotonic_dystrophy_kinase_coil.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF08826. DMPK_coil. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    ProDomi PD011252. Myotonic_dystrophy_kinase_coil. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), INVOLVEMENT IN DM1.
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), VARIANT VAL-423.
      Tissue: Brain and Muscle.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 5; 6), VARIANT VAL-423.
    4. "Decreased expression of myotonin-protein kinase messenger RNA and protein in adult form of myotonic dystrophy."
      Fu Y.-H., Friedman D.L., Richards S., Pearlman J.A., Gibbs R.A., Pizzuti A., Ashizawa T., Perryman M.B., Scarlato G., Fenwick R.G. Jr., Caskey C.T.
      Science 260:235-238(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 7; 8; 9; 10; 11 AND 12), VARIANT VAL-423.
    5. "Expression of a novel human myotonin protein kinase (MtPK) cDNA clone which encodes a protein with a thymopoietin-like domain in COS cells."
      Sasagawa N., Sorimachi H., Maruyama K., Arahata K., Ishiura S., Suzuki K.
      FEBS Lett. 351:22-26(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
      Tissue: Muscle.
    6. "Identification of rare DNA variants in mitochondrial disorders with improved array-based sequencing."
      Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R., Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W., Mindrinos M., Speed T.P., Scharfe C.
      Nucleic Acids Res. 39:44-58(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 7).
    7. "Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism."
      Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J.
      , Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.
      Nat. Commun. 5:3650-3650(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
      Tissue: Fetal brain.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Prostate.
    10. "Molecular basis of myotonic dystrophy: expansion of a trinucleotide (CTG) repeat at the 3' end of a transcript encoding a protein kinase family member."
      Brook J.D., McCurrach M., Harley H.G., Buckler A.J., Church D., Aburatani H., Hunter K., Stanton V.P., Thirion J.-P., Hudson T., Sohn R., Zemelman B., Snell R.G., Rundle S.A., Crow S., Davies J., Shelbourne P., Buxton J.
      , Jones C., Juvonen V., Johnson K., Harper P.S., Shaw D.J., Housman D.E.
      Cell 68:799-808(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-629 (ISOFORM 2), INVOLVEMENT IN DM1, VARIANT VAL-423.
    11. "Different expression of the myotonin protein kinase gene in discrete areas of human brain."
      Gennarelli M., Lucarelli M., Zelano G., Pizzuti A., Novelli G., Dallapiccola B.
      Biochem. Biophys. Res. Commun. 216:489-494(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 550-619 (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Brain.
    12. Cited for: ALTERNATIVE SPLICING, INVOLVEMENT IN DM1.
      Tissue: Brain and Heart.
    13. "MKBP, a novel member of the small heat shock protein family, binds and activates the myotonic dystrophy protein kinase."
      Suzuki A., Sugiyama Y., Hayashi Y., Nyu-i N., Yoshida M., Nonaka I., Ishiura S., Arahata K., Ohno S.
      J. Cell Biol. 140:1113-1124(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HSPB2, ENZYME REGULATION.
      Tissue: Muscle.
    14. "Myotonic dystrophy protein kinase domains mediate localization, oligomerization, novel catalytic activity, and autoinhibition."
      Bush E.W., Helmke S.M., Birnbaum R.A., Perryman M.B.
      Biochemistry 39:8480-8490(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, HOMODIMERIZATION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
    15. "Rac-1 and Raf-1 kinases, components of distinct signaling pathways, activate myotonic dystrophy protein kinase."
      Shimizu M., Wang W., Walch E.T., Dunne P.W., Epstein H.F.
      FEBS Lett. 475:273-277(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAC1, PHOSPHORYLATION BY RAF1, ENZYME REGULATION.
    16. "Constitutive and regulated modes of splicing produce six major myotonic dystrophy protein kinase (DMPK) isoforms with distinct properties."
      Groenen P.J.T.A., Wansink D.G., Coerwinkel M., van den Broek W., Jansen G., Wieringa B.
      Hum. Mol. Genet. 9:605-616(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4; 5 AND 6).
    17. Cited for: FUNCTION IN PHOSPHORYLATION OF FXYD1/PLM.
    18. "Myotonic dystrophy protein kinase phosphorylates the myosin phosphatase targeting subunit and inhibits myosin phosphatase activity."
      Muranyi A., Zhang R., Liu F., Hirano K., Ito M., Epstein H.F., Hartshorne D.J.
      FEBS Lett. 493:80-84(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PPP1R12A.
    19. "Homodimerization through coiled-coil regions enhances activity of the myotonic dystrophy protein kinase."
      Zhang R., Epstein H.F.
      FEBS Lett. 546:281-287(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMODIMERIZATION, ENZYME REGULATION.
    20. "Myotonic dystrophy protein kinase phosphorylates phospholamban and regulates calcium uptake in cardiomyocyte sarcoplasmic reticulum."
      Kaliman P., Catalucci D., Lam J.T., Kondo R., Gutierrez J.C., Reddy S., Palacin M., Zorzano A., Chien K.R., Ruiz-Lozano P.
      J. Biol. Chem. 280:8016-8021(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PLN, MUTAGENESIS OF LYS-100, INTERACTION WITH PLN.
    21. "Divergent mitochondrial and endoplasmic reticulum association of DMPK splice isoforms depends on unique sequence arrangements in tail anchors."
      van Herpen R.E., Oude Ophuis R.J., Wijers M., Bennink M.B., van de Loo F.A., Fransen J., Wieringa B., Wansink D.G.
      Mol. Cell. Biol. 25:1402-1414(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING, SUBCELLULAR LOCATION.
    22. Cited for: INVOLVEMENT IN DM1.
    23. "Chelerythrine perturbs lamellar actomyosin filaments by selective inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase."
      Tan I., Lai J., Yong J., Li S.F., Leung T.
      FEBS Lett. 585:1260-1268(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PPP1R12A.
    24. "Myotonic dystrophy protein kinase is critical for nuclear envelope integrity."
      Harmon E.B., Harmon M.L., Larsen T.D., Yang J., Glasford J.W., Perryman M.B.
      J. Biol. Chem. 286:40296-40306(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NUCLEAR ENVELOPE STABILITY, SUBCELLULAR LOCATION, INTERACTION WITH LMNA.
    25. "Crystallization and preliminary X-ray analysis of the coiled-coil domain of dystrophia myotonica kinase."
      Garcia P., Marino M., Mayans O.
      Acta Crystallogr. D 60:2336-2339(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 460-537, COILED-COIL DOMAIN.
    26. "Molecular insights into the self-assembly mechanism of dystrophia myotonica kinase."
      Garcia P., Ucurum Z., Bucher R., Svergun D.I., Huber T., Lustig A., Konarev P.V., Marino M., Mayans O.
      FASEB J. 20:1142-1151(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 460-537, SUBUNIT, COILED-COIL DOMAIN.
    27. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 11-430 IN COMPLEX WITH INHIBITOR BIM-8, SUBUNIT.
    28. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-428.

    Entry informationi

    Entry nameiDMPK_HUMAN
    AccessioniPrimary (citable) accession number: Q09013
    Secondary accession number(s): E5KR08, Q16205, Q6P5Z6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: December 14, 2011
    Last modified: October 1, 2014
    This is version 155 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3